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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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MAPK Signaling Cascades01:07

MAPK Signaling Cascades

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Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
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Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

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Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
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Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

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The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
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Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
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Updated: Sep 11, 2025

Identification of Kinase-substrate Pairs Using High Throughput Screening
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Identification of Kinase-substrate Pairs Using High Throughput Screening

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MAP2 phosphorylation: mechanisms, functional consequences, and emerging insights.

Jiali Lyu1,2, Andrew G DeMarco3, Robert A Sweet2,3,4

  • 1School of Medicine, Tsinghua Medicine, Tsinghua University, Beijing, China.

Frontiers in Cellular Neuroscience
|August 14, 2025
PubMed
Summary
This summary is machine-generated.

Microtubule-associated protein 2 (MAP2) stabilizes neuronal microtubules and dendrites. Phosphorylation by various kinases dynamically regulates MAP2 functions, impacting cytoskeletal organization and neuronal development.

Keywords:
cytoskeletondendritekinasemicrotubulemicrotubule-associated protein 2 (MAP2)phosphorylation

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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

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Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases
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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases
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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Microtubule-associated protein 2 (MAP2) is crucial for neuronal structure and function.
  • MAP2 regulates microtubule stability, dendritic morphology, and synaptic plasticity.
  • MAP2's functions are modulated by extensive phosphorylation.

Purpose of the Study:

  • To provide a comprehensive review of MAP2 structure and neuronal functions.
  • To detail the kinases that regulate MAP2 phosphorylation.
  • To highlight the impact of MAP2 phosphorylation on cellular processes.

Main Methods:

  • Literature review of MAP2 structure, function, and regulation.
  • Analysis of kinase-mediated phosphorylation sites on MAP2.
  • Synthesis of current research on MAP2's role in neuronal biology.

Main Results:

  • MAP2 stabilizes microtubules and influences dendritic outgrowth.
  • Phosphorylation dynamically alters MAP2 interactions and functions.
  • Specific kinases (Src, proline-directed, MARK, PKA, PKC, CAMKII) govern key MAP2 roles.

Conclusions:

  • MAP2 phosphorylation is a critical regulatory mechanism in neurons.
  • Understanding MAP2 phosphorylation is key to deciphering cytoskeletal dynamics and neuronal function.
  • MAP2 phosphorylation impacts cytoskeletal organization, protein chaperone activity, and dendrite development.